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LSM12_DROME
ID   LSM12_DROME             Reviewed;         217 AA.
AC   Q9VYR0; Q8T0F6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=LSM12 homolog A {ECO:0000312|FlyBase:FBgn0030364};
GN   Name=Lsm12a {ECO:0000312|FlyBase:FBgn0030364};
GN   Synonyms=Lsm12 {ECO:0000303|PubMed:28388438};
GN   ORFNames=CG15735 {ECO:0000312|FlyBase:FBgn0030364};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH TYF; ATX2 AND PABP, INTERACTION
RP   WITH TYF; ATX2 AND PABP, AND DISRUPTION PHENOTYPE.
RX   PubMed=28388438; DOI=10.1016/j.molcel.2017.03.004;
RA   Lee J., Yoo E., Lee H., Park K., Hur J.H., Lim C.;
RT   "LSM12 and ME31B/DDX6 Define Distinct Modes of Posttranscriptional
RT   Regulation by ATAXIN-2 Protein Complex in Drosophila Circadian Pacemaker
RT   Neurons.";
RL   Mol. Cell 66:129-140(2017).
CC   -!- FUNCTION: Component of the Atx2-tyf activator complex which functions
CC       in the circadian pacemaker neurons to activate the TYF-dependent
CC       translation of per and maintain 24 hour periodicity in circadian
CC       behaviors. Within the Atx2-tyf complex, likely to function as a
CC       molecular adapter which stabilizes the interaction between Atx2 and the
CC       translational regulator tyf. {ECO:0000269|PubMed:28388438}.
CC   -!- SUBUNIT: Component of the Atx2-tyf activator complex, composed of Atx2,
CC       tyf, pAbp, Lsm12. Interacts with tyf, Atx2 and pAbp.
CC       {ECO:0000269|PubMed:28388438}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in pigment dispersing
CC       factor (Pdf)-expressing clock neurons disrupts circadian locomotor
CC       rhythms, with mutants displaying long period locomotor rhythms under
CC       constant dark conditions. Enhances the period-lengthening phenotype of
CC       tyf mutants. {ECO:0000269|PubMed:28388438}.
CC   -!- SIMILARITY: Belongs to the LSM12 family. {ECO:0000305}.
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DR   EMBL; AE014298; AAF48132.2; -; Genomic_DNA.
DR   EMBL; AY069351; AAL39496.1; -; mRNA.
DR   RefSeq; NP_572777.2; NM_132549.3.
DR   AlphaFoldDB; Q9VYR0; -.
DR   BioGRID; 58572; 7.
DR   IntAct; Q9VYR0; 2.
DR   STRING; 7227.FBpp0073458; -.
DR   PaxDb; Q9VYR0; -.
DR   PRIDE; Q9VYR0; -.
DR   DNASU; 32167; -.
DR   EnsemblMetazoa; FBtr0073621; FBpp0073458; FBgn0030364.
DR   GeneID; 32167; -.
DR   KEGG; dme:Dmel_CG15735; -.
DR   UCSC; CG15735-RA; d. melanogaster.
DR   CTD; 407986; -.
DR   FlyBase; FBgn0030364; Lsm12a.
DR   VEuPathDB; VectorBase:FBgn0030364; -.
DR   eggNOG; KOG4401; Eukaryota.
DR   GeneTree; ENSGT00390000006956; -.
DR   HOGENOM; CLU_073383_2_0_1; -.
DR   InParanoid; Q9VYR0; -.
DR   OMA; WEGANIR; -.
DR   OrthoDB; 1601482at2759; -.
DR   PhylomeDB; Q9VYR0; -.
DR   BioGRID-ORCS; 32167; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 32167; -.
DR   PRO; PR:Q9VYR0; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0030364; Expressed in secondary oocyte and 25 other tissues.
DR   Genevisible; Q9VYR0; DM.
DR   GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR   GO; GO:0016070; P:RNA metabolic process; ISS:FlyBase.
DR   InterPro; IPR019181; Anticodon-binding_dom.
DR   InterPro; IPR039683; Lsm12-like.
DR   PANTHER; PTHR13542; PTHR13542; 1.
DR   Pfam; PF09793; AD; 1.
DR   SMART; SM00995; AD; 1.
PE   1: Evidence at protein level;
KW   Reference proteome.
FT   CHAIN           1..217
FT                   /note="LSM12 homolog A"
FT                   /id="PRO_0000305134"
FT   REGION          185..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   217 AA;  23746 MW;  ECF98D19700F03CA CRC64;
     MAAAAASAVN AVNDCFSIGS TVVCTTCFNE EVEGEVLAFD HNTKMLILKC RSKSTEELSD
     IYAMNLSLCS NVQVIKECNG NFDDPQKLNL EQVKMRLRKT VERRQDYLKS KNADVSPEAQ
     ELYRAIAKQY GYNEVSWQGL NIQILNEVTI SPPYRVDNVV SSSNNETSCN YIKRIIKQFF
     NTRPSPVPES GAAASTSSPS VSPTSSSLAS GSPVPAN
 
 
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